ID A0A172TEB7_9BACL Unreviewed; 2272 AA.
AC A0A172TEB7;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE RecName: Full=F5/8 type C domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=SY83_01605 {ECO:0000313|EMBL:ANE45237.1};
OS Paenibacillus swuensis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1178515 {ECO:0000313|EMBL:ANE45237.1, ECO:0000313|Proteomes:UP000076927};
RN [1] {ECO:0000313|EMBL:ANE45237.1, ECO:0000313|Proteomes:UP000076927}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DY6 {ECO:0000313|EMBL:ANE45237.1,
RC ECO:0000313|Proteomes:UP000076927};
RA Kim M.K., Srinivasan S., Lee J.-J.;
RT "Paenibacillus swuensis/DY6/whole genome sequencing.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP011388; ANE45237.1; -; Genomic_DNA.
DR RefSeq; WP_068603622.1; NZ_CP011388.1.
DR STRING; 1178515.SY83_01605; -.
DR KEGG; pswu:SY83_01605; -.
DR PATRIC; fig|1178515.4.peg.297; -.
DR OrthoDB; 9808066at2; -.
DR Proteomes; UP000076927; Chromosome.
DR GO; GO:0016787; F:hydrolase activity; IEA:InterPro.
DR CDD; cd00063; FN3; 1.
DR Gene3D; 2.60.120.1620; -; 1.
DR Gene3D; 2.60.40.1080; -; 2.
DR Gene3D; 1.20.1270.90; AF1782-like; 1.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 5.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR Gene3D; 2.160.20.10; Single-stranded right-handed beta-helix, Pectin lyase-like; 2.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR003343; Big_2.
DR InterPro; IPR002925; Dienelactn_hydro.
DR InterPro; IPR000421; FA58C.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR048482; GH141_ins.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR008964; Invasin/intimin_cell_adhesion.
DR InterPro; IPR012334; Pectin_lyas_fold.
DR InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR PANTHER; PTHR36453:SF1; BETA_HELIX DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR36453; SECRETED PROTEIN-RELATED; 1.
DR Pfam; PF02368; Big_2; 1.
DR Pfam; PF01738; DLH; 1.
DR Pfam; PF00754; F5_F8_type_C; 2.
DR Pfam; PF21231; XylC_M; 1.
DR SMART; SM00635; BID_2; 2.
DR SMART; SM00060; FN3; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR SUPFAM; SSF49265; Fibronectin type III; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 5.
DR SUPFAM; SSF49373; Invasin/intimin cell-adhesion fragments; 2.
DR SUPFAM; SSF51126; Pectin lyase-like; 1.
DR PROSITE; PS50022; FA58C_3; 3.
DR PROSITE; PS50853; FN3; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000076927}.
FT DOMAIN 27..97
FT /note="F5/8 type C"
FT /evidence="ECO:0000259|PROSITE:PS50022"
FT DOMAIN 1722..1874
FT /note="F5/8 type C"
FT /evidence="ECO:0000259|PROSITE:PS50022"
FT DOMAIN 1875..2021
FT /note="F5/8 type C"
FT /evidence="ECO:0000259|PROSITE:PS50022"
FT DOMAIN 2172..2260
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT REGION 2250..2272
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2258..2272
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2272 AA; 246100 MW; 9B1C1C38C6315D25 CRC64;
MLIKRTGMRM VSTFTVLAML FQTLLMILQP AIPAAAAAET VQNVSSNKPV TVSSRAEEAG
NLVDGNADTH WYSEWGQSSA WMKIDLGQSF QLHEIQLNAR YESTLWETVG VSVYGANQAD
YSDRVAIAQV PESGIAYSMT LPVSDTTPYR YIMLEKTIPD SLGFSEVNVM GSITQPEDAL
YTNVALGKPV TASGVLEGAY AAENGNDGNS SPMVTNWDGN AYWQVDLGRE YSIAKLQLVP
RDGIDWERRN YSILASNDAS FQESAVIGTI GSEGFDNLWN AVVTDPAPYR YVRVKTTDTK
SVGLTDFRVL VQSTAYEMAV SDLLQVVPRF SGTDIGLNEA VWTSSNQGVA SVDSSGKISA
YSKGTTTITA AYQGKTLSLP LTVKPAPEAE APTSPDLFAS FLTGQAPVVT KVISESTEGT
ISIKRVLFQS DLEEGRQNQI YALIARPTAS GSYPGLLVLH GGAGTADEGG AKEYAKRGYI
AIAPELPGIA DPNSQWASPD STGVWKSEPY GLRQLRALPD ASASSIFEAE VAALQSFYLL
KAQPEIQPGN VGMKGISWGG YTTTMVSSLL GDDVKAAYSI YGSGFYDHGS YFKGLLDGWN
RLEKMKWLKD LDAGRRAQQL TANYFVAAAT NDSYFWPTAV MDTLDRISGP VNQVFSPNDD
HTLAHLADES AQEQLYFDYH LKGEGAVPPK VQVEGSKPLA NGSIQIRFSV SGGTEVTNFK
LYYSSPDASW TTRSWTEVQA AANADGSYGA VLPAEAAAEE ADWYVFASDS RGVSASSVIY
SADSLAEQPP VVQRDTFYVS PEGDDSNEGT QESPLRTLEA ARNAVRLQTR TMKGDITVNL
RGGVYRVDGP VDFGPLDSGQ NGFQVRYQAF PGETPVIEGG KGVSGTWEPY TDGIYRIQAD
SSVLDMRELV VDGKRQQRAK SAPVKTAGIE GERTSLMVAN DLLPAGGFAF PQDLSFSMLA
QWRHYILPVS GMTRGDTYTK VNFTSEIMNT YIQNHNFDSY YNKYFIVENA LELLDEEGEW
YFDKRALVLY YKPQPGVDLN AAVIEIPQAE AFINITGLSN TKRVRNLAFQ GITFSNATWE
VVNSRGFASV QSTTIVNEKG AMEDIIPAVF NVNYADKVTI SRNTFERIGK SAINAEQGIS
DLAVTGNIFN DIAGGAVNIG STSHGTLTQA GASLPKRITV SNNVLRDIGS QFWGSAAITA
FYYDTLAIEY NDVDGANYSA ISVGWGWSGS VDSLRNLKVN YNKLFNVNRK TVDGGAVYSM
SSHVNAGLKG NYVMNVGGAF NTAALYHDQS SSGFVNEDNV VDAERGDYTS YNLNGVSNIT
ITDLYTTTGN IVNYSPGPNV RIENVHIHPD GNWPAAAQAI IAGAGLQQEY KDLLEQVKVL
LERKDIPFIR SSGVFVEDTY LFHPYSSSID RDLAKAPFEE KNGLAVFDAT EFTGYKGTEA
ADYSYLGWIN APRTGSAKYG MITHPKQMTR PVLAAPELPE LTYDIQFQTP GDYLVFVLAK
EGTVKVGFNQ QEMGTIAFPD TFAWKNGGLK VRVEQAGIHK LHIWNTNTKN AIERVVLTKA
ATAEVYENSV LPGPPTSPKA GKPSIFIPAP PAYPAFSKET GTNIAMNRPA SASSSSPGHA
PEQALDGLSI TSWRSGSADS SVWWQADLLE STPIHKLDIR FPEESTAEER RQFEVLGAND
AAFTHPVKLG EQGEEAVPPG GIASFLVEEN NGYRYVRIQK TVSGEPLALA EVKVVPSKPV
LVNVALERPV EASSGQDSAA RLVDGNKDNS TVWTSSYESE HFIRLDLLAA YRLNSIVISA
GAETESAAWN GITVYGANSE DYSDKVKLET YIKTDGGTVK VKLSGKPIYR YVLLETTSAS
AVKLSASEVE VYGVIPQPDN AIYANVAQGK PAIATSEYSD QYKAAHINDG NFNSAYVVKN
WSNDEYVQVD LGDGYAIDKI QVVPRAGNIE WERKGFAVLG SNEPDFSSAK TLGLAGGDAF
PEGEIWTAVV ADPSLYRYIR MKKTDGSGIG LAELRVLVHQ TSSRWETGKT LHLAARVLGE
DITKDNVDWK SSDSSILSVQ SDGTAKALSK GNVVITASYQ GTSVTLPVTV YKEHDTDLLE
KQITEAEEAL TNHHAGSNPG QSSSGEYSEL ARQVNDAKAV VQGAAGLPQA DIDAAADQLK
AAVSLFLKKV IVTEPLLKVT GYDKRSVSLS WTPGKVDEPV VSFILYMNGK VTKVTTASVL
TAVIQNLNKD TQYTFSIQAI NEYGHRSPLS PALQVRTKHD NGKGERTEGN GL
//
